Evidence map›Paper›PMID 27385052›Full record

ArticleScientific reports2016

Engineering de novo disulfide bond in bacterial α-type carbonic anhydrase for thermostable carbon sequestration.

Byung Hoon Jo, Tae Yoon Park, Hyun June Park, Young Joo Yeon, Young Je Yoo, Hyung Joon Cha

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
3.8field-weighted citation impact, top 6% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

15 citing papers in PubMed, 50 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Directed evolution of an ultrastable carbonic anhydrase fromComputational and structural biotechnology journal · 2025
    Article
  5. Article
  6. In Silico Analysis of Glucose Oxidase fromBioengineering (Basel, Switzerland) · 2021
    Article
  7. Article
  8. Article
  9. Overexpression and Purification ofFrontiers in plant science · 2020
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. FoldX as Protein Engineering Tool: Better Than Random Based Approaches?Computational and structural biotechnology journal · 2018
    Review
  15. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 2 institutions in 1 country.

Byung Hoon JoDepartment of Chemical Engineering, Pohang University of Science and Technology, Pohang 790-784, Korea.
Tae Yoon ParkDepartment of Chemical Engineering, Pohang University of Science and Technology, Pohang 790-784, Korea.
Hyun June ParkBio-Max Institute, Seoul National University, Seoul 151-742, Korea.
Young Joo YeonThe Institute of Molecular Biology and Genetics, Seoul National University, Seoul 151-742, Korea.
Young Je YooBio-Max Institute, Seoul National University, Seoul 151-742, Korea.
Hyung Joon ChaDepartment of Chemical Engineering, Pohang University of Science and Technology, Pohang 790-784, Korea.
Pohang University of Science and Technology · KRSeoul National University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Exploiting carbonic anhydrase (CA), an enzyme that rapidly catalyzes carbon dioxide hydration, is an attractive biomimetic route for carbon sequestration due to its environmental compatibility and potential economic viability. However, the industrial applications of CA are strongly hampered by the unstable nature of enzymes. In this work, we introduced in silico designed, de novo disulfide bond in a bacterial α-type CA to enhance thermostability. Three variants were selected and expressed in Escherichia coli with an additional disulfide bridge. One of the variants showed great enhancement in terms of both kinetic and thermodynamic stabilities. This improvement could be attributed to the loss of conformational entropy of the unfolded state, showing increased rigidity. The variant showed an upward-shifted optimal temperature and appeared to be thermoactivated, which compensated for the lowered activity at 25 °C. Collectively, the variant constructed by the rapid and effective de novo disulfide engineering can be used as an efficient biocatalyst for carbon sequestration under high temperature conditions.

Indexed as

Carbonic AnhydrasesCarbon SequestrationCatalytic DomainDisulfidesEscherichia coliKineticsTemperatureThermodynamicsCarbonic AnhydrasesDisulfides

Identifiers

PMID27385052
PMCPMC4935852
OpenAlexW2471705234

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.